4PFX

The highly conserved domain of unknown function 1792 has a distinct glycosyltransferase fold

Summary for 4PFX

• Entry DOI: 10.2210/pdb4pfx/pdb
• Descriptor: Putative glycosyltransferase (GalT1), URIDINE-5'-DIPHOSPHATE, ACETATE ION, ... (4 entities in total)
• Functional Keywords: duf1792, glycosyltransferase, transferase
• Biological source: Streptococcus parasanguinis
• Total number of polymer chains: 1
• Total formula weight: 32524.66

Authors

Zhang, H.,Wu, H. (deposition date: 2014-04-30, release date: 2014-07-23, Last modification date: 2024-10-23)

Primary citation

Zhang, H.,Zhu, F.,Yang, T.,Ding, L.,Zhou, M.,Li, J.,Haslam, S.M.,Dell, A.,Erlandsen, H.,Wu, H.
The highly conserved domain of unknown function 1792 has a distinct glycosyltransferase fold.
Nat Commun, 5:4339-4339, 2014

PubMed Abstract: More than 33,000 glycosyltransferases have been identified. Structural studies, however, have only revealed two distinct glycosyltransferase (GT) folds, GT-A and GT-B. Here we report a 1.34-Å resolution X-ray crystallographic structure of a previously uncharacterized 'domain of unknown function' 1792 (DUF1792) and show that the domain adopts a new fold and is required for glycosylation of a family of serine-rich repeat streptococcal adhesins. Biochemical studies reveal that the domain is a glucosyltransferase, and it catalyses the transfer of glucose to the branch point of the hexasaccharide O-linked to the serine-rich repeat of the bacterial adhesin, Fap1 of Streptococcus parasanguinis. DUF1792 homologues from both Gram-positive and Gram-negative bacteria also exhibit the activity. Thus, DUF1792 represents a new family of glycosyltransferases; therefore, we designate it as a GT-D glycosyltransferase fold. As the domain is highly conserved in bacteria and not found in eukaryotes, it can be explored as a new antibacterial target.

PubMed: 25023666
DOI: 10.1038/ncomms5339

Experimental method

X-RAY DIFFRACTION (1.66 Å)